ID J9DXK9_9PROT Unreviewed; 608 AA.
AC J9DXK9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phosphogluconate dehydratase {ECO:0000256|HAMAP-Rule:MF_02094};
DE EC=4.2.1.12 {ECO:0000256|HAMAP-Rule:MF_02094};
GN Name=edd {ECO:0000256|HAMAP-Rule:MF_02094};
GN ORFNames=IMCC14465_18390 {ECO:0000313|EMBL:EJW20414.1};
OS alpha proteobacterium IMCC14465.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW20414.1, ECO:0000313|Proteomes:UP000004836};
RN [1] {ECO:0000313|EMBL:EJW20414.1, ECO:0000313|Proteomes:UP000004836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW20414.1,
RC ECO:0000313|Proteomes:UP000004836};
RX PubMed=23209213; DOI=10.1128/JB.01888-12;
RA Yang S.J., Kang I., Cho J.C.;
RT "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT to the PS1 Clade of Alphaproteobacteria.";
RL J. Bacteriol. 194:6952-6953(2012).
CC -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000256|HAMAP-
CC Rule:MF_02094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-
CC gluconate + H2O; Xref=Rhea:RHEA:17277, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57569, ChEBI:CHEBI:58759; EC=4.2.1.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02094};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02094};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02094};
CC -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02094}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486, ECO:0000256|HAMAP-Rule:MF_02094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW20414.1}.
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DR EMBL; ALYF01000012; EJW20414.1; -; Genomic_DNA.
DR AlphaFoldDB; J9DXK9; -.
DR STRING; 1220535.IMCC14465_18390; -.
DR PATRIC; fig|1220535.3.peg.1829; -.
DR eggNOG; COG0129; Bacteria.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00226; -.
DR Proteomes; UP000004836; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004456; F:phosphogluconate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR HAMAP; MF_02094; Edd; 1.
DR InterPro; IPR004786; 6-phosphgluc_deHydtase.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR NCBIfam; TIGR01196; edd; 1.
DR PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR PANTHER; PTHR43661:SF1; PHOSPHOGLUCONATE DEHYDRATASE; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02094};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02094};
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064, ECO:0000256|HAMAP-
KW Rule:MF_02094}; Iron {ECO:0000256|HAMAP-Rule:MF_02094};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02094};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02094};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02094};
KW Reference proteome {ECO:0000313|Proteomes:UP000004836}.
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ SEQUENCE 608 AA; 65552 MW; 9964C02B1266CFB6 CRC64;
MTHKKIIEIT EKITARSQAS RKNYLDMIEA AQTAHHEKGL SAGNVAHATA ACPVADKKSM
IAGDWAHLAI ITAYNDMLSA HQPYERYPEL IRGFAREFNA TTQVAGGVPA MCDGVTQGQP
GMELSLFSRD VIAMSTAIAL SHNTFEAAIY LGICDKIVPG LLMGALQFGH LPSIFIPSGP
MPSGLANEEK SRVRKAYARG EASREELLAT EMKSYHSAGT CTFYGTANSN QMLMEIMGLH
VPGAAFIPPE TDIRDALTRE AVKQLVENAQ KSKTKNRLAD IVTEKSIVNA MIGLLATGGS
TNHTIHLPAI ARAAGIHINW DDFDELSQVI PLICKIYPNG KADINQFHAA GGMSYVIRTL
LDNGYLHADV KTVLGDGLES FATEPVLQGG EIEWRDGPLT SGDDSIISDA QTPFSKNGGL
RTVSGNLGRG VVKISAVKHE HYIITAPARV FYDQNDVVTA FENSELERDV IIVLIGQGPK
SNGMPELHKL TPPLGSLLEK GFNVALVTDG RMSGASGAVP AAIQITPEAA DNGFLTRIKD
GDMICLDCEK ATLTNLAEDF NKRENLHDKA FKPSENTTYQ TMGRNLFAPL RNVVSGAESG
GSIFFEEM
//
